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Information on EC 3.2.1.155 - xyloglucan-specific exo-beta-1,4-glucanase
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EC Tree
3.2.1.155 xyloglucan-specific exo-beta-1,4-glucanaseIUBMB Comments
The enzyme removes branched oligosaccharides, containing preferentially four glucoside residues in the main chain, from xyloglucan molecules in a processive manner after the initial endo-type attack on a polysaccharide [1-5]. Hydrolysis occurs at either the unsubstituted D-glucopyranose residue in the main backbone and/or the D-glucopyranose residue bearing a xylosyl group [1-5]. The enzyme does not display activity, or shows very low activity, towards other beta-D-glucans [1,2,4,5].
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
Synonyms
xyloglucanase xgh74a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cel74A
EC 3.2.1.160
-
-
formerly
-
XEG74
XG
xyloglucanase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
endo-type reaction mode, overview
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Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
exo-type reaction mode, overview
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Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
exo-type reaction mode, overview
Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
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-
-
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SYSTEMATIC NAME
IUBMB Comments
[(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan exo-glucohydrolase
The enzyme removes branched oligosaccharides, containing preferentially four glucoside residues in the main chain, from xyloglucan molecules in a processive manner after the initial endo-type attack on a polysaccharide [1-5]. Hydrolysis occurs at either the unsubstituted D-glucopyranose residue in the main backbone and/or the D-glucopyranose residue bearing a xylosyl group [1-5]. The enzyme does not display activity, or shows very low activity, towards other beta-D-glucans [1,2,4,5].
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CAS REGISTRY NUMBER
COMMENTARY
1000598-79-7
-
76901-10-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl xyloglucan derivatives + H2O
oligosaccharides
artificial substrate
-
-
?
carboxymethylcellulose + H2O
carboxymethyl cellulose oligosaccharides
-
-
-
?
tamarind xyloglucan + H2O
oligosaccharides
highly specific for, exo-type reaction
with end products XXXG, XXLG/XLXG, and XLLG
-
?
xyloglucan + H2O
?
Xgh74 contributes to the in vivo degradation of the hemicellulose xyloglucan and xylan by the cellulosome of Clostridium thermocellum
-
-
?
xyloglucan + H2O
cellotetraose
tamarind xyloglucan. Xgh74A hydrolyzes every fourth beta-1,4-glucan bond in the xyloglucan backbone, thus producing decorated cellotetraose units
-
-
?
beta-glucan + H2O
beta-glucan oligosaccharides
8% of the activity with xyloglucan
-
-
?
beta-glucan + H2O
beta-glucan oligosaccharides
-
8% of the activity with xyloglucan
-
-
?
beta-glucan + H2O
beta-glucan oligosaccharides
8% of the activity with xyloglucan
-
-
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose oligosaccharides
5% of the activity with xyloglucan
-
-
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose oligosaccharides
-
5% of the activity with xyloglucan
-
-
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose oligosaccharides
6% of the activity with xyloglucan
-
-
?
tamarind xyloglucan + H2O
oligosacchrides
-
highly specific for, endo-type reaction
with end products XXXG, XXLG/XLXG, and XLLG
-
?
tamarind xyloglucan + H2O
oligosacchrides
-
highly specific for, exo-type reaction
with end products XXXG, XXLG/XLXG, and XLLG
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
the enzyme is a true endo-glucanase when it acts on linear substrates without bulky substituents in the polymer backbone. When the enzyme acts on polymeric substrate with bulky side chains, its mode of action is switched to exo-like
XXXG, XXLG and XLLG oligosaccharides
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
-
the enzyme is a true endo-glucanase when it acts on linear substrates without bulky substituents in the polymer backbone. When the enzyme acts on polymeric substrate with bulky side chains, its mode of action is switched to exo-like
XXXG, XXLG and XLLG oligosaccharides
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
XEG74 has dual endo-mode and exo-mode activities
-
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
XEG74 has dual endo-mode and exo-mode activities
-
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
-
XXXG, XXLG and XLLG oligosaccharides
-
?
additional information
?
-
-
low activity on carboxymethyl cellulose and on glucuronoxylan. Lack of activity on amorphous cellulose
-
-
?
additional information
?
-
low activity on carboxymethyl cellulose and on glucuronoxylan. Lack of activity on amorphous cellulose
-
-
?
additional information
?
-
-
substrate specificity, carboxymethylcellulose and barley beta-glucan are poor or no substrates
-
-
?
additional information
?
-
-
substrate specificity, carboxymethylcellulose and barley beta-glucan are poor or no substrates
-
-
?
additional information
?
-
no activity towards Avicel, carboxymethylcellulose, barley beta-1,3/1,4-glucan or xylan
-
-
?
additional information
?
-
no activity towards Avicel, carboxymethylcellulose, barley beta-1,3/1,4-glucan or xylan
-
-
?
additional information
?
-
substrate specificity, carboxymethylcellulose and barley beta-glucan are poor or no substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
xyloglucan + H2O
?
Xgh74 contributes to the in vivo degradation of the hemicellulose xyloglucan and xylan by the cellulosome of Clostridium thermocellum
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
KM-value for xyloglucan is 0.3 mg/ml, KM-value for beta-glucan is 8 mg/ml, KM-value for carboxymethylcellulose is above 51 mg/mL
-
additional information
additional information
-
KM-value for xyloglucan is 0.31 mg/ml, KM-value for beta-glucan is 18 mg/ml, KM-value for carboxymethylcellulose is above 50 mg/mL
-
additional information
additional information
KM-value for xyloglucan is 1.2 mg/ml
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
6.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.3 - 6.9
more than 50% of maximal activity in the pH-range 4.5-7.2
4.5 - 7.2
-
more than 50% of maximal activity in the pH-range 4.5-7.2
5.7 - 7.8
5.7 - 7.8
more than 50% of maximal activity in the pH-range 5.7-7.8, hydrolysis of tamarind seed xyloglucan
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
4.1 - 4.3
4.1 - 4.3
isoelectrofocusing, there may be different forms of the enzyme resulting from O-glycosylation
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). XG74_HYPJQ
Hypocrea jecorina (strain QM6a)
838
0
87133
Swiss-Prot
Secretory Pathway (Reliability: 3)
M5C9Y8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
713
0
75552
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1W2TM66_ROSNE
832
0
86087
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1W2TAW4_ROSNE
842
0
89602
TrEMBL
Secretory Pathway (Reliability: 2)
M5CBF0_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
139
0
15262
TrEMBL
other Location (Reliability: 2)
A0A084FYA9_PSEDA
842
0
88630
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0F8CR49_CERFI
838
0
87373
TrEMBL
Secretory Pathway (Reliability: 1)
A0A084FYA1_PSEDA
843
0
89999
TrEMBL
Secretory Pathway (Reliability: 5)
XG74_ACETH
842
0
92393
Swiss-Prot
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 75000-105000, isoelectrofocusing, there may be different forms of the enzyme resulting from O-glycosylation, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
enzyme contains two putative N-glycosylation sites. There may be different forms of the enzyme resulting from O-glycosylation
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
60
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
further purification of the commercial preparation, by ion exchange chromatography, to homogeneity
recombinant
further purification of the commercial preparation, by ion exchange chromatography, to homogeneity
-
further purification of the commercial preparation, by ion exchange chromatography, to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
both the cane molasses medium and lactose-based conventional medium can serve as excellent growth media for Trichoderma reesei. The most abundant cellulolytic enzymes identified in both media are cellobiohydrolases (Cel7A/Cel6A) and endoglucanases (Cel7A/Cel5A) and are more abundant in CMM. Both media can serve as an inducer of xylanolytic enzymes. The main xylanases (XYNI/XYNIV) and xyloglucanase (Cel74A) are found at higher concentrations in the the cane molasses medium than lactose-based conventional medium
synthesis
-
both the cane molasses medium and lactose-based conventional medium can serve as excellent growth media for Trichoderma reesei. The most abundant cellulolytic enzymes identified in both media are cellobiohydrolases (Cel7A/Cel6A) and endoglucanases (Cel7A/Cel5A) and are more abundant in CMM. Both media can serve as an inducer of xylanolytic enzymes. The main xylanases (XYNI/XYNIV) and xyloglucanase (Cel74A) are found at higher concentrations in the the cane molasses medium than lactose-based conventional medium
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grishutin, S.G.; Gusakov, A.V.; Markov, A.V.; Ustinov, B.B.; Semenova, M.V.; Sinitsyn, A.P.
Specific xyloglucanases as a new class of polysaccharide-degrading enzymes
Biochim. Biophys. Acta
1674
268-281
2004
Aspergillus japonicus, Chrysosporium lucknowense, Trichoderma reesei (Q7Z9M8)
brenda
Yaoi, K.; Nakai, T.; Kameda, Y.; Hiyoshi, A.; Mitsuishi, Y.
Cloning and characterization of two xyloglucanases from Paenibacillus sp. strain KM21
Appl. Environ. Microbiol.
71
7670-7678
2005
Paenibacillus sp. (Q3MUH7), Paenibacillus sp. KM21 (Q3MUH7)
brenda
Zverlov, V.V.; Schantz, N.; Schmitt-Kopplin, P.; Schwarz, W.H.
Two new major subunits in the cellulosome of Clostridium thermocellum: xyloglucanase Xgh74A and endoxylanase Xyn10D
Microbiology
151
3395-3401
2005
Acetivibrio thermocellus, Acetivibrio thermocellus (Q70DK5)
brenda
He, J.; Wu, A.; Chen, D.; Yu, B.; Mao, X.; Zheng, P.; Yu, J.; Tian, G.
Cost-effective lignocellulolytic enzyme production by Trichoderma reesei on a cane molasses medium
Biotechnol. Biofuels
7
43
2014
Trichoderma reesei (Q7Z9M8), Trichoderma reesei QM6a (Q7Z9M8)
brenda
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Release 2023.1 (January 2023)
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